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The heregulin family of polypeptides arise as splice variants
from a single gene and share a conserved epidermal growth factor
(EGF)-like domain thought to be the major determinant of their
biological activities. We report here the cloning of a novel member of
this family, termed sensory and motor neuron-derived factor or SMDF,
which is highly expressed in sensory and motor neurons in human and
rodent species. It contains a C-terminal
Volume 270,
Number 24,
Issue of June 16, pp. 14523-14532, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
A NOVEL HEREGULIN VARIANT HIGHLY EXPRESSED IN SENSORY AND MOTOR
NEURONS
-type EGF-like domain and
an unique N-terminal sequence which lacks an Ig-like domain and is
distinct from all known heregulin variants. Mammalian cell-expressed
SMDF activates tyrosine phosphorylation of a 185-kDa protein in cell
lines expressing p185, indicating
that it is biologically active. Analyses of expression patterns suggest
that, unlike other heregulin variants, SMDF is expressed mainly in the
nervous system. In situ hybridization signals with the unique
SMDF sequence probe and with a probe to the conserved EGF-like domain
are comparable, suggesting that SMDF is the predominant isoform
expressed in sensory and motor neurons. Expression of SMDF is
maintained in both adult motor neurons and dorsal root ganglion
neurons. These findings suggest that SMDF may mediate biological
responses such as Schwann cell proliferation and acetylcholine receptor
induction in the peripheral nervous system.
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